Structural Basis for Iron Piracy by Pathogenic Neisseria

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Please use this identifier to cite or link to this item: http://hdl.handle.net/1853/45213

Title: Structural Basis for Iron Piracy by Pathogenic Neisseria
Author: Buchanan, Susan
Abstract: Neisseria are obligate human pathogens causing bacterial meningitis, septicemia, and gonorrhea. Neisseria require iron for survival and can extract it directly from human transferrin for transport across the outer membrane. The transport system consists of TbpA, an integral outer membrane protein, and TbpB, a co-receptor attached to the cell surface; both proteins are potentially important vaccine and therapeutic targets. Two key questions driving Neisseria research are: 1) how human transferrin is specifically targeted, and 2) how the bacteria liberate iron from transferrin at neutral pH. To address them, we solved crystal structures of the TbpA-transferrin complex and of the corresponding co-receptor TbpB. We characterized the TbpB-transferrin complex by small angle X-ray scattering and the TbpA-TbpB-transferrin complex by electron microscopy. Collectively, our studies provide a rational basis for the specificity of TbpA for human transferrin, show how TbpA promotes iron release from transferrin, and elucidate how TbpB facilitates this process.
Description: Susan Buchanan of the National Institutes of Health presented a lecture on Tuesday, October 16, 2012 from 11:00 am to 12:00 pm in the Klaus Advanced Computing Building, Room 1116E. Runtime: 52:04 minutes.
Type: Lecture
Video
URI: http://hdl.handle.net/1853/45213
Date: 2012-10-16
Contributor: National Institutes of Health (U.S.)
Publisher: Georgia Institute of Technology
Subject: Protein crystallography
Bacterial pathogens
Host-pathogen interactions

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